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Links from Protein

Items: 11

1.

Rubredoxin metal binding domain

This is the C-terminal rubredoxin metal binding domain found in Interest in lipopolysaccharide (LPS) assembly protein B (LapB) . Rubredoxin proteins form small non-heme iron binding sites that use four cysteine residues to coordinate a single metal ion in a tetrahedral environment. Rubredoxins are most commonly found in bacterial systems, but have also been found in eukaryotes. The key features of these rubredoxin-like domains are the extended loops or 'knuckles' and the tetracysteine mode of iron binding. Structural analysis of LapB from Escherichia coli show that the rubredoxin metal binding domain is intimately bound to the TPR motifs and that this association to the TPR motifs is essential to LPS regulation and growth in vivo [1]. Other family members include RadA proteins which play a role in DNA damage repair. In E. coli, a protein known as RadA (or Sms) participates in the recombinational repair of radiation-damaged DNA in a process that uses an undamaged DNA strand in one DNA duplex to fill a DNA strand gap in a homologous sister DNA duplex. RadA carries a zinc finger at the N-terminal domain [2]. [1]. 26190574. An Unexpected Duo: Rubredoxin Binds Nine TPR Motifs to Form. LapB, an Essential Regulator of Lipopolysaccharide Synthesis.. Prince C, Jia Z;. Structure. 2015;23:1500-1506.. [2]. 28581365. Fine Epitope Mapping of Monoclonal Antibodies to the DNA Repair. Protein, RadA.. Stuart MK, Hudman DA, Nachtrab SN, Hiatt JL, Seo J, Pullen SJ,. Sargentini NJ;. Monoclon Antib Immunodiagn Immunother. 2017;36:83-94. (from Pfam)

Date:
2024-08-14
Family Accession:
NF037181.5
Method:
HMM
2.

AAA family ATPase

This AAA domain is found in a wide variety of presumed DNA repair proteins. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024872.5
Method:
HMM
3.

AAA family ATPase

GO Terms:
Molecular Function:
ATP hydrolysis activity (GO:0016887)
Date:
2024-08-14
Family Accession:
NF024793.5
Method:
HMM
4.

ATPase domain-containing protein

This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria [1]. [1]. 10064581. Physical interactions among circadian clock proteins KaiA, KaiB. and KaiC in cyanobacteria.. Iwasaki H, Taniguchi Y, Ishiura M, Kondo T;. EMBO J 1999;18:1137-1145. (from Pfam)

Date:
2024-08-14
Family Accession:
NF018455.5
Method:
HMM
5.

AAA family ATPase

AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2]. [1]. 7646486. A 200-amino acid ATPase module in search of a basic function.. Confalonieri F, Duguet M;. Bioessays 1995;17:639-650.. A large extension of the family. [2]. 9927482. AAA+: A class of chaperone-like ATPases associated with the. assembly, operation, and disassembly of protein complexes.. Neuwald AF, Aravind L, Spouge JL, Koonin EV;. Genome Res 1999;9:27-43. (from Pfam)

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Molecular Function:
ATP hydrolysis activity (GO:0016887)
Date:
2024-08-14
Family Accession:
NF012234.5
Method:
HMM
6.
new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.
new record, indexing in progress
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